Nucleotide sequences of the sfuA, sfuB, and sfuC genes of Serratia marcescens suggest a periplasmic-binding-protein-dependent iron transport mechanism
| Autor: | Volkmar Braun, Sibylle Gaisser, Annemarie Angerer |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
DNA
Bacterial Iron Molecular Sequence Data Restriction Mapping Biology Microbiology Gene product Bacterial Proteins Sequence Homology Nucleic Acid Consensus sequence Amino Acid Sequence Codon Site-directed mutagenesis Molecular Biology Gene Serratia marcescens Base Sequence Nucleic acid sequence Membrane Proteins Biological Transport Periplasmic space Membrane protein Biochemistry Genes Bacterial Periplasmic Binding Proteins Carrier Proteins Oligonucleotide Probes Plasmids Research Article |
| Zdroj: | Journal of Bacteriology. 172:572-578 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.172.2.572-578.1990 |
| Popis: | The cloned sfu region of the Serratia marcescens chromosome confers the ability to grow on iron-limited media to an Escherichia coli K-12 strain that is unable to synthesize a siderophore. This DNA fragment was sequenced and found to contain three genes termed sfuA, sfuB, and sfuC, arranged and transcribed in that order. The sfuA gene encoded a periplasmic polypeptide with calculated molecular weights of 36,154 for the precursor and 33,490 for the mature protein. The sfuB gene product was a very hydrophobic protein with a molecular weight of 56,589. The sfuC gene was found to encode a rather polar but membrane-bound protein with a molecular weight of 36,671 which exhibited strong homology to consensus sequences of nucleotide-binding proteins. The number, structural characteristics, and locations of the SfuABC proteins were typical of a periplasmic-binding-protein-dependent transport mechanism. How Fe3+ is solubilized and taken up across the outer membrane remains an enigma. |
| Databáze: | OpenAIRE |
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